MMP19_MOUSE
ID MMP19_MOUSE Reviewed; 527 AA.
AC Q9JHI0; Q8C360;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Matrix metalloproteinase-19;
DE Short=MMP-19;
DE EC=3.4.24.-;
DE AltName: Full=Matrix metalloproteinase RASI;
DE Flags: Precursor;
GN Name=Mmp19; Synonyms=Rasi;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C3H/HeJ;
RX PubMed=11092553; DOI=10.1023/a:1007196529604;
RA Caterina J.J., Shi J., Kozak C.A., Engler J.A., Birkedal-Hansen H.;
RT "Characterization, expression analysis and chromosomal mapping of mouse
RT matrix metalloproteinase-19 (MMP-19).";
RL Mol. Biol. Rep. 27:73-79(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hurskainen T., Seldin M.F., Pendas A., Lopez-Otin C., Apte S.S.;
RT "Mmp19 encodes a GPI anchored matrix metalloprotease expressed in
RT musculoskeletal, neural and epithelial tissues.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129/Ola;
RX PubMed=11054540; DOI=10.1016/s0378-1119(00)00369-3;
RA Mueller M.S., Harnasch M., Kolb C., Kusch J., Sadowski T., Sedlacek R.;
RT "The murine ortholog of matrix metalloproteinase 19: its cloning, gene
RT organization, and expression.";
RL Gene 256:101-111(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 54-527.
RC STRAIN=C57BL/6J; TISSUE=Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
CC -!- FUNCTION: Endopeptidase that degrades various components of the
CC extracellular matrix, such as aggrecan and cartilage oligomeric matrix
CC protein (comp), during development, haemostasis and pathological
CC conditions (arthritic disease). May also play a role in
CC neovascularization or angiogenesis (By similarity). Hydrolyzes collagen
CC type IV, laminin, nidogen, nascin-C isoform, fibronectin, and type I
CC gelatin (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}; Extracellular side {ECO:0000305}. Secreted,
CC extracellular space, extracellular matrix {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the liver. Expressed in the
CC arterial tunica media of large blood vessels.
CC -!- DEVELOPMENTAL STAGE: Expressed in proliferating chondrocytes in the
CC chondroepiphysis during musculoskeletal development.
CC -!- DOMAIN: The conserved cysteine present in the cysteine-switch motif
CC binds the catalytic zinc ion, thus inhibiting the enzyme. The
CC dissociation of the cysteine from the zinc ion upon the activation-
CC peptide release activates the enzyme.
CC -!- PTM: Activated by autolytic cleavage after Lys-98. {ECO:0000250}.
CC -!- PTM: Tyrosine phosphorylated by PKDCC/VLK.
CC {ECO:0000250|UniProtKB:Q99542}.
CC -!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
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DR EMBL; AF155221; AAF73292.1; -; mRNA.
DR EMBL; AF162446; AAF80464.1; -; mRNA.
DR EMBL; AF153199; AAG29880.1; -; mRNA.
DR EMBL; AK086808; BAC39747.1; -; mRNA.
DR CCDS; CCDS24292.1; -.
DR RefSeq; NP_067387.1; NM_021412.3.
DR AlphaFoldDB; Q9JHI0; -.
DR SMR; Q9JHI0; -.
DR STRING; 10090.ENSMUSP00000026411; -.
DR MEROPS; M10.021; -.
DR GlyGen; Q9JHI0; 4 sites.
DR iPTMnet; Q9JHI0; -.
DR PhosphoSitePlus; Q9JHI0; -.
DR MaxQB; Q9JHI0; -.
DR PaxDb; Q9JHI0; -.
DR PRIDE; Q9JHI0; -.
DR ProteomicsDB; 291476; -.
DR Antibodypedia; 2017; 487 antibodies from 36 providers.
DR DNASU; 58223; -.
DR Ensembl; ENSMUST00000026411; ENSMUSP00000026411; ENSMUSG00000025355.
DR GeneID; 58223; -.
DR KEGG; mmu:58223; -.
DR UCSC; uc007hof.1; mouse.
DR CTD; 4327; -.
DR MGI; MGI:1927899; Mmp19.
DR VEuPathDB; HostDB:ENSMUSG00000025355; -.
DR eggNOG; KOG1565; Eukaryota.
DR GeneTree; ENSGT00940000158593; -.
DR HOGENOM; CLU_015489_8_3_1; -.
DR InParanoid; Q9JHI0; -.
DR OMA; RTDFSHY; -.
DR OrthoDB; 1075463at2759; -.
DR PhylomeDB; Q9JHI0; -.
DR TreeFam; TF315428; -.
DR Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR BioGRID-ORCS; 58223; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Mmp19; mouse.
DR PRO; PR:Q9JHI0; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9JHI0; protein.
DR Bgee; ENSMUSG00000025355; Expressed in liver and 103 other tissues.
DR ExpressionAtlas; Q9JHI0; baseline and differential.
DR Genevisible; Q9JHI0; MM.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; ISS:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0030574; P:collagen catabolic process; IBA:GO_Central.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0001554; P:luteolysis; IEA:Ensembl.
DR GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
DR GO; GO:0001542; P:ovulation from ovarian follicle; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
DR GO; GO:0009725; P:response to hormone; IEA:Ensembl.
DR CDD; cd00094; HX; 1.
DR CDD; cd04278; ZnMc_MMP; 1.
DR Gene3D; 2.110.10.10; -; 2.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR000585; Hemopexin-like_dom.
DR InterPro; IPR036375; Hemopexin-like_dom_sf.
DR InterPro; IPR018487; Hemopexin-like_repeat.
DR InterPro; IPR018486; Hemopexin_CS.
DR InterPro; IPR033739; M10A_MMP.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR028724; MMP19.
DR InterPro; IPR001818; Pept_M10_metallopeptidase.
DR InterPro; IPR021190; Pept_M10A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR PANTHER; PTHR10201:SF166; PTHR10201:SF166; 1.
DR Pfam; PF00045; Hemopexin; 4.
DR Pfam; PF00413; Peptidase_M10; 1.
DR Pfam; PF01471; PG_binding_1; 1.
DR PIRSF; PIRSF001191; Peptidase_M10A_matrix; 1.
DR PRINTS; PR00138; MATRIXIN.
DR SMART; SM00120; HX; 4.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF47090; SSF47090; 1.
DR SUPFAM; SSF50923; SSF50923; 1.
DR PROSITE; PS00024; HEMOPEXIN; 1.
DR PROSITE; PS51642; HEMOPEXIN_2; 4.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Angiogenesis; Calcium; Cell membrane; Collagen degradation;
KW Developmental protein; Differentiation; Disulfide bond;
KW Extracellular matrix; Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein;
KW Membrane; Metal-binding; Metalloprotease; Phosphoprotein; Protease;
KW Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..98
FT /evidence="ECO:0000250"
FT /id="PRO_0000028828"
FT CHAIN 99..512
FT /note="Matrix metalloproteinase-19"
FT /id="PRO_0000028829"
FT PROPEP 513..527
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000028830"
FT REPEAT 286..333
FT /note="Hemopexin 1"
FT REPEAT 334..372
FT /note="Hemopexin 2"
FT REPEAT 377..425
FT /note="Hemopexin 3"
FT REPEAT 426..471
FT /note="Hemopexin 4"
FT REGION 473..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 84..91
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT ACT_SITE 214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /note="in inhibited form"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT LIPID 512
FT /note="GPI-anchor amidated aspartate"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 479
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 521
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 289..471
FT /evidence="ECO:0000250"
SQ SEQUENCE 527 AA; 59122 MW; 8AD0AE41A1CD335E CRC64;
MDWQQLWLAF LLPMTVSGRA LGPTEKEAVL DYLLQYGYLQ KPLEGADDFR LEDITEALRT
FQEASGLPIS GQMDDATRAR MKQPRCGLED PFNQKSLKYL LLGHWRKKNL TFRIFNVPST
LSLPRVRAAL HQAFKYWSSV APLTFREVKA GWADIRLSFH GRQSLYCSNT FDGPGKVLAH
ADIPELGSIH FDKDELWTEG TYQGVNLRII AAHEVGHALG LGHSRYTQAL MAPVYAGYQP
FFKLHPDDVA GIQALYGKRS PETRDEEEET EMLTVSPVTA KPGPMPNPCS GEVDAMVLGP
RGKTYAFKGD YVWTVTDSGP GPLFQISALW EGLPGNLDAA VYSPRTRRTH FFKGNKVWRY
VDFKMSPGFP MKFNRVEPNL DAALYWPVNQ KVFLFKGSGY WQWDELARTD LSRYPKPIKE
LFTGVPDRPS AAMSWQDGQV YFFKGKEYWR LNQQLRVAKG YPRNTTHWMH CGSQTPDTNS
STGDVTPSTT DTVLGTTPST MGSTLDIPSA TDSASLSFSA NVTLLGA
